glu c protease  (Worthington Biochemical)


Bioz Verified Symbol Worthington Biochemical is a verified supplier
Bioz Manufacturer Symbol Worthington Biochemical manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93
    Name:
    Protease S Aureus Endoproteinase Glu C
    Description:
    Chromatographically purified according to Drapeau G Boily Y and Houmard J J Biol Chem 247 6720 1972 A lyophilized powder
    Catalog Number:
    ls003605
    Price:
    228
    Source:
    S. aureus V8
    Size:
    5 mg
    Cas Number:
    66676.43.5
    Buy from Supplier


    Structured Review

    Worthington Biochemical glu c protease
    Phosphorylation sites identified by each approach. (a) Total number of distinct phosphorylation sites by method. Each experimental approach identified a larger number of phosphorylation sites than <t>Glu-C</t> only workflows. (b) Comparison of unique phosphorylation
    Chromatographically purified according to Drapeau G Boily Y and Houmard J J Biol Chem 247 6720 1972 A lyophilized powder
    https://www.bioz.com/result/glu c protease/product/Worthington Biochemical
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    glu c protease - by Bioz Stars, 2021-03
    93/100 stars

    Images

    1) Product Images from "Increasing phosphoproteomic coverage through sequential digestion by complementary proteases"

    Article Title: Increasing phosphoproteomic coverage through sequential digestion by complementary proteases

    Journal: Analytical and bioanalytical chemistry

    doi: 10.1007/s00216-011-5466-5

    Phosphorylation sites identified by each approach. (a) Total number of distinct phosphorylation sites by method. Each experimental approach identified a larger number of phosphorylation sites than Glu-C only workflows. (b) Comparison of unique phosphorylation
    Figure Legend Snippet: Phosphorylation sites identified by each approach. (a) Total number of distinct phosphorylation sites by method. Each experimental approach identified a larger number of phosphorylation sites than Glu-C only workflows. (b) Comparison of unique phosphorylation

    Techniques Used:

    Experimental design and analysis of sequential digestion workflows. (a) Schematic diagram of the three sequential digestion approaches. GSPT closely resembles the traditional workflow with substitution of Glu-C for initial digestion and trypsin digestion
    Figure Legend Snippet: Experimental design and analysis of sequential digestion workflows. (a) Schematic diagram of the three sequential digestion approaches. GSPT closely resembles the traditional workflow with substitution of Glu-C for initial digestion and trypsin digestion

    Techniques Used:

    Evaluation of a Glu-C only based phosphoproteomic workflow. (a) In the traditional phosphoproteomic workflow, proteins are obtained from cell lysates and proteolytically digested with trypsin. The resultant peptides are separated into fractions via strong
    Figure Legend Snippet: Evaluation of a Glu-C only based phosphoproteomic workflow. (a) In the traditional phosphoproteomic workflow, proteins are obtained from cell lysates and proteolytically digested with trypsin. The resultant peptides are separated into fractions via strong

    Techniques Used:

    2) Product Images from "Increasing phosphoproteomic coverage through sequential digestion by complementary proteases"

    Article Title: Increasing phosphoproteomic coverage through sequential digestion by complementary proteases

    Journal: Analytical and bioanalytical chemistry

    doi: 10.1007/s00216-011-5466-5

    Phosphorylation sites identified by each approach. (a) Total number of distinct phosphorylation sites by method. Each experimental approach identified a larger number of phosphorylation sites than Glu-C only workflows. (b) Comparison of unique phosphorylation
    Figure Legend Snippet: Phosphorylation sites identified by each approach. (a) Total number of distinct phosphorylation sites by method. Each experimental approach identified a larger number of phosphorylation sites than Glu-C only workflows. (b) Comparison of unique phosphorylation

    Techniques Used:

    Experimental design and analysis of sequential digestion workflows. (a) Schematic diagram of the three sequential digestion approaches. GSPT closely resembles the traditional workflow with substitution of Glu-C for initial digestion and trypsin digestion
    Figure Legend Snippet: Experimental design and analysis of sequential digestion workflows. (a) Schematic diagram of the three sequential digestion approaches. GSPT closely resembles the traditional workflow with substitution of Glu-C for initial digestion and trypsin digestion

    Techniques Used:

    Evaluation of a Glu-C only based phosphoproteomic workflow. (a) In the traditional phosphoproteomic workflow, proteins are obtained from cell lysates and proteolytically digested with trypsin. The resultant peptides are separated into fractions via strong
    Figure Legend Snippet: Evaluation of a Glu-C only based phosphoproteomic workflow. (a) In the traditional phosphoproteomic workflow, proteins are obtained from cell lysates and proteolytically digested with trypsin. The resultant peptides are separated into fractions via strong

    Techniques Used:

    3) Product Images from "Increasing phosphoproteomic coverage through sequential digestion by complementary proteases"

    Article Title: Increasing phosphoproteomic coverage through sequential digestion by complementary proteases

    Journal: Analytical and bioanalytical chemistry

    doi: 10.1007/s00216-011-5466-5

    Phosphorylation sites identified by each approach. (a) Total number of distinct phosphorylation sites by method. Each experimental approach identified a larger number of phosphorylation sites than Glu-C only workflows. (b) Comparison of unique phosphorylation
    Figure Legend Snippet: Phosphorylation sites identified by each approach. (a) Total number of distinct phosphorylation sites by method. Each experimental approach identified a larger number of phosphorylation sites than Glu-C only workflows. (b) Comparison of unique phosphorylation

    Techniques Used:

    Experimental design and analysis of sequential digestion workflows. (a) Schematic diagram of the three sequential digestion approaches. GSPT closely resembles the traditional workflow with substitution of Glu-C for initial digestion and trypsin digestion
    Figure Legend Snippet: Experimental design and analysis of sequential digestion workflows. (a) Schematic diagram of the three sequential digestion approaches. GSPT closely resembles the traditional workflow with substitution of Glu-C for initial digestion and trypsin digestion

    Techniques Used:

    Evaluation of a Glu-C only based phosphoproteomic workflow. (a) In the traditional phosphoproteomic workflow, proteins are obtained from cell lysates and proteolytically digested with trypsin. The resultant peptides are separated into fractions via strong
    Figure Legend Snippet: Evaluation of a Glu-C only based phosphoproteomic workflow. (a) In the traditional phosphoproteomic workflow, proteins are obtained from cell lysates and proteolytically digested with trypsin. The resultant peptides are separated into fractions via strong

    Techniques Used:

    Related Articles

    Modification:

    Article Title: Increasing phosphoproteomic coverage through sequential digestion by complementary proteases
    Article Snippet: .. Modified trypsin was from Promega (Madison, WI); Glu-C protease was from Worthington Biochemicals (Lakewood, NJ). .. Urea, Tris-HCl, CaCl2 , ammonium bicarbonate (NH4 HCO3 ), sodium fluoride (NaCl), potassium fluoride (KCl), potassium phosphate (KH2 PO4 ), phosphoric acid, sodium ortho-vanadate, sodium molybdate, sodium tartrate, beta-glycerophosphate, DL-dithiothreitol, iodoacetamide were from Sigma-Aldrich (St. Louis, MO).

    Activity Assay:

    Article Title: Structural and Functional Characterization of Mature Forms of Metalloprotease E495 from Arctic Sea-Ice Bacterium Pseudoalteromonas sp. SM495
    Article Snippet: .. The protease activity to gelatin was determined with the method provided by Worthington Biochemical Co. . .. The degradation ability of E495-M and E495-M-C1 to CPC, APC and gamma globulin were analyzed using SDS-PAGE.

    Incubation:

    Article Title: Identification of a region in the coiled-coil domain of Smc3 that is essential for cohesin activity
    Article Snippet: .. Smc3-3V5 or smc3-L217P-3V5 were precipitated from asynchronous cell cultures and incubated with V8 protease, with or without ATP. .. The reaction products were analyzed by western blot with antibodies against V5.

    Article Title: Identification of a region in the coiled-coil domain of Smc3 that is essential for cohesin activity
    Article Snippet: Chromatin immunoprecipitation (ChIP) Chromatin immunoprecipitation (ChIP) was performed as described ( ). .. Limited proteolysis Immunoprecipitated Smc3-3V5, either wild-type or L217P, were incubated in 20 μl of buffer (50 mM Tris–HCl (pH 8.0) and 1 mM MgCl2 ) with 5 mg/ml V8 protease (Worthington Biochemical), with or without 1 mM ATP (Sigma). ..

    other:

    Article Title: Increasing phosphoproteomic coverage through sequential digestion by complementary proteases
    Article Snippet: Briefly, a single, large pool of NCI-H23 cells were lysed in 8M urea, and their proteins were digested using Glu-C protease, desalted, and lyophilized in three equal (5mg) aliquots.

    Immunoprecipitation:

    Article Title: Identification of a region in the coiled-coil domain of Smc3 that is essential for cohesin activity
    Article Snippet: Chromatin immunoprecipitation (ChIP) Chromatin immunoprecipitation (ChIP) was performed as described ( ). .. Limited proteolysis Immunoprecipitated Smc3-3V5, either wild-type or L217P, were incubated in 20 μl of buffer (50 mM Tris–HCl (pH 8.0) and 1 mM MgCl2 ) with 5 mg/ml V8 protease (Worthington Biochemical), with or without 1 mM ATP (Sigma). ..

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93
    Worthington Biochemical v8 protease
    Proteolytic cleavage of Smc3 wild-type and mutant proteins. Smc3-V5 and smc3-L217P-3V5 were pulled down by using antibodies against V5. The precipitated proteins were washed and incubated with <t>V8</t> protease at 23°C in the absence ( A ) or presence ( B ) of 1 mM ATP. The reactions were stopped at the indicated time points. The cleaved products were resolved by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and analyzed by western blot, using antibody against V5. The major cleaved products discussed in the text are labeled as a–e. * indicates a non-specific band. A representative experiment is shown. ( n = 4).
    V8 Protease, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/v8 protease/product/Worthington Biochemical
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    v8 protease - by Bioz Stars, 2021-03
    93/100 stars
      Buy from Supplier

    Image Search Results


    Proteolytic cleavage of Smc3 wild-type and mutant proteins. Smc3-V5 and smc3-L217P-3V5 were pulled down by using antibodies against V5. The precipitated proteins were washed and incubated with V8 protease at 23°C in the absence ( A ) or presence ( B ) of 1 mM ATP. The reactions were stopped at the indicated time points. The cleaved products were resolved by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and analyzed by western blot, using antibody against V5. The major cleaved products discussed in the text are labeled as a–e. * indicates a non-specific band. A representative experiment is shown. ( n = 4).

    Journal: Nucleic Acids Research

    Article Title: Identification of a region in the coiled-coil domain of Smc3 that is essential for cohesin activity

    doi: 10.1093/nar/gkw539

    Figure Lengend Snippet: Proteolytic cleavage of Smc3 wild-type and mutant proteins. Smc3-V5 and smc3-L217P-3V5 were pulled down by using antibodies against V5. The precipitated proteins were washed and incubated with V8 protease at 23°C in the absence ( A ) or presence ( B ) of 1 mM ATP. The reactions were stopped at the indicated time points. The cleaved products were resolved by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and analyzed by western blot, using antibody against V5. The major cleaved products discussed in the text are labeled as a–e. * indicates a non-specific band. A representative experiment is shown. ( n = 4).

    Article Snippet: Smc3-3V5 or smc3-L217P-3V5 were precipitated from asynchronous cell cultures and incubated with V8 protease, with or without ATP.

    Techniques: Mutagenesis, Incubation, Polyacrylamide Gel Electrophoresis, Western Blot, Labeling

    Phosphorylation sites identified by each approach. (a) Total number of distinct phosphorylation sites by method. Each experimental approach identified a larger number of phosphorylation sites than Glu-C only workflows. (b) Comparison of unique phosphorylation

    Journal: Analytical and bioanalytical chemistry

    Article Title: Increasing phosphoproteomic coverage through sequential digestion by complementary proteases

    doi: 10.1007/s00216-011-5466-5

    Figure Lengend Snippet: Phosphorylation sites identified by each approach. (a) Total number of distinct phosphorylation sites by method. Each experimental approach identified a larger number of phosphorylation sites than Glu-C only workflows. (b) Comparison of unique phosphorylation

    Article Snippet: Modified trypsin was from Promega (Madison, WI); Glu-C protease was from Worthington Biochemicals (Lakewood, NJ).

    Techniques:

    Experimental design and analysis of sequential digestion workflows. (a) Schematic diagram of the three sequential digestion approaches. GSPT closely resembles the traditional workflow with substitution of Glu-C for initial digestion and trypsin digestion

    Journal: Analytical and bioanalytical chemistry

    Article Title: Increasing phosphoproteomic coverage through sequential digestion by complementary proteases

    doi: 10.1007/s00216-011-5466-5

    Figure Lengend Snippet: Experimental design and analysis of sequential digestion workflows. (a) Schematic diagram of the three sequential digestion approaches. GSPT closely resembles the traditional workflow with substitution of Glu-C for initial digestion and trypsin digestion

    Article Snippet: Modified trypsin was from Promega (Madison, WI); Glu-C protease was from Worthington Biochemicals (Lakewood, NJ).

    Techniques:

    Evaluation of a Glu-C only based phosphoproteomic workflow. (a) In the traditional phosphoproteomic workflow, proteins are obtained from cell lysates and proteolytically digested with trypsin. The resultant peptides are separated into fractions via strong

    Journal: Analytical and bioanalytical chemistry

    Article Title: Increasing phosphoproteomic coverage through sequential digestion by complementary proteases

    doi: 10.1007/s00216-011-5466-5

    Figure Lengend Snippet: Evaluation of a Glu-C only based phosphoproteomic workflow. (a) In the traditional phosphoproteomic workflow, proteins are obtained from cell lysates and proteolytically digested with trypsin. The resultant peptides are separated into fractions via strong

    Article Snippet: Modified trypsin was from Promega (Madison, WI); Glu-C protease was from Worthington Biochemicals (Lakewood, NJ).

    Techniques: